1phm

X-ray diffraction
1.9Å resolution

PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT

Released:

Function and Biology Details

Reactions catalysed:
[Peptide]-glycine + 2 ascorbate + O(2) = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H(2)O
[Peptide]-(2S)-2-hydroxyglycine = [peptide]-amide + glyoxylate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidylglycine alpha-amidating monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 34.58 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P14925 (Residues: 45-354; Coverage: 33%)
Gene name: Pam
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 68.4Å b: 68.66Å c: 81.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.261
Expression system: Cricetulus griseus